Research workbench
Htra proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues
Analyse Htra proteases are activated by a conserved mechanism that can be triggered by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MH5
- Type
- protein
- Length
- 393 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease do
- EC
- 3.4.21.-
- UniProt
- P0C0V0
- Ligands
- DFP
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease do (EC 3.4.21.-) | protein | 191 | 16% helix, 40% strand | P0C0V0 |
| B | Protease do (EC 3.4.21.-) | protein | 202 | 15% helix, 43% strand | P0C0V0 |
Ligands and binding sites
- DFP · Diisopropyl phosphonate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.29 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 540 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 3MH5 · HtrA proteases are activated by a conserved mechanism that can be triggered by distinct… · the same entry in another collection · chain A against A, TM-score 1.00
- P0C0V0 · AlphaFold monomer V2.0 prediction for periplasmic serine endoprotease degp (P0C0V0) · a predicted model of the same protein · chain B against A, TM-score 0.95
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0C0V0
- Elsewhere: RCSB PDB 3MH5 · PDBe 3MH5 · UniProt P0C0V0
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